Differential characterization of two leucine aminopeptidases in Drosophila melanogaster.
Two leucine aminopeptidases from Drosophila melanogaster larvae have been partially purified. The LAP A and D enzymes have similar biochemical characteristics including molecular weights of approximately equal to 280,000 daltons. Michaelis-Menten constants of approximately equal to 0.05 mM, associations with metal cofactors, and specificities toward natural and chromogenic substrates. They differ in their pH optima and spatial distributions. If the closely linked genes that code for these enzymes have resulted from a tandem gene duplication event, it is suggested that there has been subsequent evolutionary divergence. This would provide Drosophila larvae with two related, but functionally distinct enzymes.
D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology*; D004592:Electrophoresis, Starch Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007814:Larva; D007931:Leucyl Aminopeptidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D013379:Substrate Specificity
D007931:Leucyl Aminopeptidase